GA201: A Novel Humanized and Glycoengineered Anti-EGFR Antibody—Response

  title={GA201: A Novel Humanized and Glycoengineered Anti-EGFR Antibody—Response},
  author={Christian A. Gerdes and Pablo Uma{\~n}a},
  journal={Clinical Cancer Research},
  pages={1055 - 1055}
We are pleased that Dr. Modjtahedi found our work on GA201 interesting. The origin of the CDR sequences of GA201 based on the published sequences of the ICR62 antibody is clearly mentioned in our publication ([1][1]). Likewise, previous publications describing the properties of ICR62 were also cited 

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GA201 (RG7160): A Novel, Humanized, Glycoengineered Anti-EGFR Antibody with Enhanced ADCC and Superior In Vivo Efficacy Compared with Cetuximab
The data suggest that GA201 may be more effective than cetuximab in patients with EGFR-positive solid tumors and may also represent a first-in-class treatment of patients with KRAS-mutated tumors.
Phase I pharmacokinetic and pharmacodynamic dose-escalation study of RG7160 (GA201), the first glycoengineered monoclonal antibody against the epidermal growth factor receptor, in patients with advanced solid tumors.
RG7160 had an acceptable safety profile with manageable AEs and demonstrated promising efficacy in this heavily pretreated patient cohort and a marked reduction in circulating natural killer cells and increased infiltration of immune effector cells into skin rash were seen.
The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms.
The structural model predicts that only one of the two Fc-fucose residues needs to be absent for increased binding affinity toward FcgammaRIII, and can be exploited for the design of new antibodies with altered Fc receptor binding affinity and enhanced therapeutic potential.
Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucose
A detailed, molecular understanding of the regulatory role of Fc-oligosaccharide core fucosylation in improving ADCC is obtained and a unique mechanism by which the immune system can regulate antibody-mediated effector functions is suggested.
Br€ unker P, Uma~ na P. The carbohydrate at FcgRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
  • J Biol Chem
  • 2006
Authors' Affiliation: Roche Glycart AG, pRED